NLTPC_RICCO
ID NLTPC_RICCO Reviewed; 116 AA.
AC P10975; Q43120;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Non-specific lipid-transfer protein C, cotyledon-specific isoform;
DE Short=NS-LTP C;
DE AltName: Full=Phospholipid transfer protein;
DE Short=PLTP;
DE Flags: Precursor;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling cotyledon;
RX PubMed=1783615; DOI=10.1093/oxfordjournals.jbchem.a123666;
RA Tsuboi S., Suga T., Takishima K., Mamiya G., Matsui K., Ozeki Y.,
RA Yamada M.;
RT "Organ-specific occurrence and expression of the isoforms of nonspecific
RT lipid transfer protein in castor bean seedlings, and molecular cloning of a
RT full-length cDNA for a cotyledon-specific isoform.";
RL J. Biochem. 110:823-831(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Weig A., Komor E.;
RT "The lipid-transfer protein C of Ricinus communis L.: isolation of two cDNA
RT sequences which are strongly and exclusively expressed in cotyledons after
RT germination.";
RL Planta 187:367-371(1992).
RN [3]
RP PROTEIN SEQUENCE OF 25-116.
RC TISSUE=Seed;
RX PubMed=3191918; DOI=10.1111/j.1432-1033.1988.tb14368.x;
RA Takishima K., Watanabe S., Yamada M., Suga T., Mamiya G.;
RT "Amino acid sequences of two nonspecific lipid-transfer proteins from
RT germinated castor bean.";
RL Eur. J. Biochem. 177:241-249(1988).
CC -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC phospholipids as well as galactolipids across membranes. May play a
CC role in wax or cutin deposition in the cell walls of expanding
CC epidermal cells and certain secretory tissues.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; D11077; BAA01802.1; -; mRNA.
DR EMBL; M86354; AAA33877.1; -; mRNA.
DR PIR; S01796; S01796.
DR PIR; T10084; T10084.
DR PIR; T10098; T10098.
DR AlphaFoldDB; P10975; -.
DR SMR; P10975; -.
DR STRING; 3988.XP_002533769.1; -.
DR eggNOG; ENOG502S1F3; Eukaryota.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33076; PTHR33076; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
DR PROSITE; PS00597; PLANT_LTP; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Lipid-binding; Signal;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:3191918"
FT CHAIN 25..116
FT /note="Non-specific lipid-transfer protein C, cotyledon-
FT specific isoform"
FT /id="PRO_0000018405"
FT DISULFID 28..76
FT DISULFID 38..53
FT /evidence="ECO:0000305"
FT DISULFID 54..98
FT /evidence="ECO:0000305"
FT DISULFID 74..112
FT VARIANT 66
FT /note="T -> S"
FT CONFLICT 4
FT /note="V -> A (in Ref. 2; AAA33877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 12262 MW; 45287C7EA7BD7681 CRC64;
MKNVVFSVLL LLSFLFCLAN TNEAAVPCST VDMKAAACVG FATGKDSKPS QACCTGLQQL
AQTVKTVDDK KAICRCLKAS SKSLGIKDQF LSKIPAACNI KVGFPVSTNT NCETIH
